› 5brq

X-ray diffraction
2Å resolution

Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA)

Released:
DOI: 10.2210/pdb5brq/pdb
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Source organism: Bacillus licheniformis DSM 13 = ATCC 14580
Primary publication:
Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity.
Lin MG, Chi MC, Naveen V, Li YC, Lin LL, Hsiao CD
Acta Crystallogr D Struct Biol 72 59-70 (2016)
PMID: 26894535

Function and Biology Details

Reaction catalysed: 
Alpha,alpha-trehalose 6-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha,alpha-phosphotrehalase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 568 amino acids
Theoretical weight: 66.64 KDa
Source organism: Bacillus licheniformis DSM 13 = ATCC 14580
Expression system: Escherichia coli M15
UniProt:
  • Canonical: Q65MI2 (Residues: 1-562; Coverage: 100%)
Gene names: BL03069, treA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P1
Unit cell:
a: 59.802Å b: 97.584Å c: 108.336Å
α: 98.2° β: 91.44° γ: 108.15°
R-values:
R R work R free
0.182 0.181 0.245
Expression system: Escherichia coli M15

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Citations

1 review citation

Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.
Sardiña-Peña et al. (2023)
2 other articles

4 mentions without citation

Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-α-glucosidases.
Miyazaki et al. (2020)
3 more

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